P2C04_ARATH
ID P2C04_ARATH Reviewed; 662 AA.
AC Q9LQN6; Q8LFF0; Q9ASX4;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Probable protein phosphatase 2C 4;
DE Short=AtPP2C04;
DE EC=3.1.3.16;
DE AltName: Full=Protein POLTERGEIST-LIKE 5;
DE AltName: Full=Protein phosphatase 2C PLL5;
DE Short=PP2C PLL5;
GN Name=PLL5; OrderedLocusNames=At1g07630; ORFNames=F24B9.25, F24B9.31;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16112663; DOI=10.1016/j.ydbio.2005.06.020;
RA Song S.-K., Clark S.E.;
RT "POL and related phosphatases are dosage-sensitive regulators of meristem
RT and organ development in Arabidopsis.";
RL Dev. Biol. 285:272-284(2005).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19021904; DOI=10.1186/1471-2164-9-550;
RA Xue T., Wang D., Zhang S., Ehlting J., Ni F., Jacab S., Zheng C., Zhong Y.;
RT "Genome-wide and expression analysis of protein phosphatase 2C in rice and
RT Arabidopsis.";
RL BMC Genomics 9:550-550(2008).
CC -!- FUNCTION: Involved in leaf development regulation.
CC {ECO:0000269|PubMed:16112663}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, leaves, stems, young
CC inflorescences, flowers and siliques. {ECO:0000269|PubMed:16112663}.
CC -!- DOMAIN: The conserved PP2C phosphatase domain (250-651) is interrupted
CC by an insertion of approximately 100 amino acids.
CC -!- DISRUPTION PHENOTYPE: Plants show abnormal leaves altered in shape and
CC curling. {ECO:0000269|PubMed:16112663}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK32783.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAM91433.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC007583; AAF75095.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28151.1; -; Genomic_DNA.
DR EMBL; AF361615; AAK32783.1; ALT_FRAME; mRNA.
DR EMBL; AY133603; AAM91433.1; ALT_FRAME; mRNA.
DR EMBL; AY084887; AAM61450.1; -; mRNA.
DR PIR; G86210; G86210.
DR RefSeq; NP_563791.1; NM_100636.3.
DR AlphaFoldDB; Q9LQN6; -.
DR SMR; Q9LQN6; -.
DR STRING; 3702.AT1G07630.1; -.
DR iPTMnet; Q9LQN6; -.
DR PaxDb; Q9LQN6; -.
DR PRIDE; Q9LQN6; -.
DR ProteomicsDB; 248699; -.
DR EnsemblPlants; AT1G07630.1; AT1G07630.1; AT1G07630.
DR GeneID; 837276; -.
DR Gramene; AT1G07630.1; AT1G07630.1; AT1G07630.
DR KEGG; ath:AT1G07630; -.
DR Araport; AT1G07630; -.
DR TAIR; locus:2026605; AT1G07630.
DR eggNOG; KOG0700; Eukaryota.
DR HOGENOM; CLU_013173_12_1_1; -.
DR InParanoid; Q9LQN6; -.
DR OMA; CEWEREK; -.
DR OrthoDB; 461546at2759; -.
DR PhylomeDB; Q9LQN6; -.
DR PRO; PR:Q9LQN6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LQN6; baseline and differential.
DR Genevisible; Q9LQN6; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR PANTHER; PTHR13832; PTHR13832; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Nucleus; Phosphoprotein; Protein phosphatase; Reference proteome.
FT CHAIN 1..662
FT /note="Probable protein phosphatase 2C 4"
FT /id="PRO_0000301263"
FT DOMAIN 249..653
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT BINDING 286
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 581
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 644
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8RWN7"
FT CONFLICT 368
FT /note="S -> G (in Ref. 4; AAM61450)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 662 AA; 74274 MW; B1A3670D06B1B94E CRC64;
MGNGVTKLSI CFTGGGGERL RPKDISVLLP DPLDEGLGHS FCYVRPDPTL ISSSKVHSEE
DTTTTTFRTI SGASVSANTA TPLSTSLYDP YGHIDRAAAF ESTTSFSSIP LQPIPKSSGP
IVLGSGPIER GFLSGPIERG FMSGPLDRVG LFSGPLDKPN SDHHHQFQRS FSHGLALRVG
SRKRSLVRIL RRAISKTMSR GQNSIVAPIK SVKDSDNWGI RSEKSRNLHN ENLTVNSLNF
SSEVSLDDDV SLENQNLQWA QGKAGEDRVH VVVSEEHGWL FVGIYDGFNG PDAPDYLLSH
LYPVVHRELK GLLWDDSNVE SKSQDLERSN GDESCSNQEK DETCERWWRC EWDRESQDLD
RRLKEQISRR SGSDRLTNHS EVLEALSQAL RKTEEAYLDT ADKMLDENPE LALMGSCVLV
MLMKGEDIYV MNVGDSRAVL GQKSEPDYWL AKIRQDLERI NEETMMNDLE GCEGDQSSLV
PNLSAFQLTV DHSTNIEEEV ERIRNEHPDD VTAVTNERVK GSLKVTRAFG AGFLKQPKWN
NALLEMFQID YVGKSPYINC LPSLYHHRLG SKDRFLILSS DGLYQYFTNE EAVSEVELFI
TLQPEGDPAQ HLVQELLFRA AKKAGMDFHE LLEIPQGERR RYHDDVSIVV ISLEGRMWKS
CV
